Detail Information for IndEnz0002018569
IED ID IndEnz0002018569
Enzyme Type ID protease018569
Protein Name Disintegrin and metalloproteinase domain-containing protein 10 homolog
ADAM 10 homolog
EC 3.4.24.81
Gene Name sup-17 DY3.7
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MSSPIRNRLQLVVTLIFCLFFENVNGLNNFIDNFETLNYRATHVANQVTRRKRSIDSAASHYQEPIGFRFNAYNRTFHVQLHPIDDSLFHEDHMSDVDGGYADIKPSHFLYEGYLKDDPNSHVHGSVFDGVFEGHIQTGEGRRYSIDKAAKYFERDDRPTQYHSIIYRDDEINHRKWRVKRDAENLSEQMQGCGFSSRVRREMTDVQNSGESTDFFTNYMTMGGRSKRANTLRDHDGLYFVRTCSLYMQADHKLYEHIRMKEGNNDPIRTREEIVSLFYNHIKAVNEIYEGTNFNGIKGLHFVIQRTSIYTPDSCDRGRAKTDSDNPFCEENVDVSNFLNLNSQRNHSAFCLAYALTFRDFVGGTLGLAWVASPQFNTAGGICQVHQRYNEGSRGWVYRSLNTGIVTLVNYGNRVPARVSQLTLAHEIGHNFGSPHDFPAECQPGLPDGNFIMFASATSGDKPNNGKFSPCSVKNISAVLAVVLKSMPVDPTRNASPVGIGKRNCFQERTSAFCGNQIYEPGEECDCGFSQADCDQMGDKCCVPHEARGNGGPGPCKRKPGAQCSPSQGYCCNPDTCSLHGKNEEKICRQESECSNLQTCDGRNAQCPVSPPKHDGIPCQDSTKVCSSGQCNGSVCAMFGLEDCFLTEGKADELCFLACIKDGKCTSSVHLPEFSANRTNFLQNMRKDKPGLILHPGSPCNNYKGYCDIFRKCRSVDANGPLARLKNLLFNKRTIETLTQWAQDNWWVVGVGGLVFLVIMALFVKCCAVHTPSTNPNKPPALNIYQTLTRPGTLIRQHRQRHRAAAGSVPPGPGAQPRSGAASAPSRTTPSARPSAPPLVAPQVAVAVPPGVVGPPIPLIATHPGSSSSTPAVIVLEPPPPYTAADPGSAMGGPRRGHRKNKRQTSSDAAGSSGNGGKKKGK
Enzyme Length 922
Uniprot Accession Number G5EFD9
Absorption
Active Site ACT_SITE 427; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81; Evidence={ECO:0000250|UniProtKB:O14672};
DNA Binding
EC Number 3.4.24.81
Enzyme Function FUNCTION: Metalloprotease (By similarity). Acts together with protease adm-4 and in a cell autonomous manner to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision and vulva precursor cell specification (PubMed:9428412, PubMed:9409830, PubMed:16197940). By modulating glp-1/Notch signaling, plays a role in germline development (PubMed:16197940). Probably by modulating BMP-like Sma/Mab signaling via the shedding of unc-40 ectodomain, involved in the regulation of body size and mesoderm development (PubMed:28068334). Probably by shedding ephrin efn-4, regulates axon guidance of SDQL neuron during development (PubMed:26903502). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:16197940, ECO:0000269|PubMed:26903502, ECO:0000269|PubMed:28068334, ECO:0000269|PubMed:9409830, ECO:0000269|PubMed:9428412}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (10); Domain (2); Glycosylation (6); Metal binding (3); Mutagenesis (2); Propeptide (1); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;Cleavage on pair of basic residues;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Note=Localizes to the basolateral cell membrane in embryos. {ECO:0000269|PubMed:28068334}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11559592; 17897480; 21085631; 21177967; 22004469; 22286215; 22500807; 22560298; 23800452; 25487147; 28669545;
Motif
Gene Encoded By
Mass 101,573
Kinetics
Metal Binding METAL 426; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 430; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 436; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276
Rhea ID
Cross Reference Brenda